ID W5TK68_9NOCA Unreviewed; 1819 AA.
AC W5TK68;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative acyl-CoA carboxylase {ECO:0000313|EMBL:AHH19559.1};
GN ORFNames=NONO_c47750 {ECO:0000313|EMBL:AHH19559.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH19559.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH19559.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH19559.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006850; AHH19559.1; -; Genomic_DNA.
DR RefSeq; WP_025350955.1; NZ_CP006850.1.
DR STRING; 1415166.NONO_c47750; -.
DR KEGG; nno:NONO_c47750; -.
DR PATRIC; fig|1415166.3.peg.4916; -.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_239133_0_0_11; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000019150; Chromosome.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000019150}.
FT DOMAIN 1..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 572..655
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1537..1819
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1819 AA; 197631 MW; F6868B1183DDB25D CRC64;
MFSRIAIVNR GEAAMRLIHA VRDLAAATAR QIETVALYTD VDRNATFVRE ADIAYDLGPA
SARPYLDLKA LEKALVTTKA DAAWVGWGFV AEDPAFAELC DHIGITFIGP SADAMRKLGD
KIGAKLIAEE VGVPVAPWSR GAVETLDAAI AYAAEVGYPL MLKATAGGGG RGIRVITNEA
ELVDAYERTS QEAARAFGSG VVFLERLVTG ARHVEVQVIA DGQGTAWALG VRDCSVQRRN
QKVIEESASP VLRPEQVADL KSSAERLAVA VGYRGAATVE FLYHPGDELF AFLEVNTRLQ
VEHPITEYTT GFDLVRAQLH VASGGRLEGE PPAERGHAIE ARLNAEDPDR DFAPAPGRIA
LLDLPAGPGI RVDTGVSQGD TIPADFDSMI AKIIAYGSDR EQALGRLRRA VGETRVIIEG
GATNKSFVLD LLDQPEVIDA SADTGWIDRV RGEGRLVAQR HTAVALAAAA IDAYEQEERA
ERERLLSTAA GGRPQVQHES GRPLDLKLRG VSYRLRVARV GAHRFRIGIE AGGDIHTADV
DLLRFDRHTG QIVVNGIRYR LVTGTHGPTI VVDVDGVTHR VSRDEGGVVR SPAPALVVAK
PLEVGDEVEA GAPVLVLESM KMETVLRAPF KGRLKECGVS VGSQVEAGAP LLRLEPIADD
EEDAAEAQTA DAVELDLPAA PTQVLAHDRT VRGQEDLRGL LLGFDVDPHD DRRVLADYLV
ARKDAIADNR RPLAEELELV ELFTDLAELT HNRFRGEDAH NHVHSAREYF HTYLQSLDVE
RAGLPEFYRA GLAKALGHYG VAELDRTPEL EAAVFRIFLA QQRPSDTVNV VTALLREWLN
EPVPDRVLQE PVGLALERLV AATQVRFPVI ADLTRGLVYA WYGQPLLRRN RARVYSTVRK
HLSHLDAQPD AADRSERIAE MVRSTEPLVR LLAQRLDRGI PDNTVMLEVL TRRYYGNKGL
TGVRTEEVDG CTFVVAERRG VSLVSAAVGF DALDTVLGGL GELAGGAASI EADIYLGWEN
QPEDFDAMAS ALQEVLGAKA LPGQVHRITA TVAGSGGAVM HHHFTFRPTS TGLVEERLIR
GLHPYIAERM QMRRLRKFDL TRLPSSDEEV YLFQGVAKEN PADERLIAFA QVRDLTALRE
HDGRLLSLPT AESTVATCVD SIRRAQSRRP SRKRFHTNRI VLYIWPPLDV TRAELDTIVS
RVEPTTAGAG LEEVLLIARQ PDADTGELEK IVVRIRFDAT GGTEVTVGER TDDPVEPLDE
YRQKVLRASS RNTVYPYELT GLLGDFAEYD LDENHALVPV DRPKGRNTAA IVAGVVSTPT
ERHPEGVTRV VLLGDPTRSL GALSEPECRR VIAALDLAEQ MRVPLEWFSL SSGARISMKS
GTENMDWVAA ALKRIVEFTQ DGGEINIVVS GINVGAQPYW NAEATMLMHT KGILVMTPDS
AMVLTGKQAL DFSGGVSAED NFGIGGYDRV MGPNGQAQYW APNLAGARDV LMSHYDHTYI
APGEATPRRA QTTDPVDRDV CAFPHIVPES DFTTVGEIFS ATANPDRKKP FDIRTVMRAL
SDQDHPVLER WAGMADAETA VVQDAHLGGI PVCLLGIESR GVPRRGFPST DGPDTYTAGT
LFPRSSKKAA RAINAASGNR PLVVLANLSG FDGSPESMRK LQLEYGAEIG RAIVNFRGPI
VFCVISRYHG GAFVVFSKAL NPNMTVLALE GSFASVLGGA PAAAVVFAGE VDTRTASDPR
VRELESRVAN ASGTERAEAS AELDELRSTV RAEKLGEVAA EFDRVHNIHR AVEVGSVDAV
ISARELRPRI IEAIESRTA
//